Proteomics

Dataset Information

0

Complexome profiling of heart mitochondria from mouse expressing alternative oxidase

ABSTRACT: Ciona intestinalis alternative oxidase (AOX) is a mitochondrial respiratory enzyme that acts as an alternative electron sink for ubiquinol (reduced quinone) when the cytochrome bc1 complex (complex III) and/or cytochrome c oxidase (complex IV) are inhibited or impaired (El-Khoury et al., 2014). AOX thus enables electron flux through the mitochondrial electron transport chain (ETC) and thereby prevents reverse electron transport from succinate dehydrogenase (complex II) to NADH:ubiquinone oxidoreductase (complex I) and mitochondrial ROS production, restores redox balance and Krebs cycle activity. As a non-proton-motive enzyme, however, AOX does not directly support ATP production. Previously, a mouse model was generated that despite ubiquitous expression of AOX revealed no deviations from normal physiology and which now is used as model to test mitochondrial disease paradigms (Szibor et al., 2017).

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Heart

SUBMITTER: Ilka Wittig  

LAB HEAD: Marten Szibor

PROVIDER: PXD014016 | Pride | 2019-12-13

REPOSITORIES: Pride

Json Xml

Dataset's files

Source:
Action DRS
142603JMAOXTissueAOX01.RAW Raw
142603JMAOXTissueAOX02.RAW Raw
142603JMAOXTissueAOX03.RAW Raw
142603JMAOXTissueAOX04.RAW Raw
142603JMAOXTissueAOX05.RAW Raw
Items per page:
1 - 5 of 98
altmetric image

Publications

Bioenergetic consequences from xenotopic expression of a tunicate AOX in mouse mitochondria: Switch from RET and ROS to FET.

Szibor Marten M   Gainutdinov Timur T   Fernandez-Vizarra Erika E   Dufour Eric E   Gizatullina Zemfira Z   Debska-Vielhaber Grazyna G   Heidler Juliana J   Wittig Ilka I   Viscomi Carlo C   Gellerich Frank F   Moore Anthony L AL  

Biochimica et biophysica acta. Bioenergetics 20191209 2

Electron transfer from all respiratory chain dehydrogenases of the electron transport chain (ETC) converges at the level of the quinone (Q) pool. The Q redox state is thus a function of electron input (reduction) and output (oxidation) and closely reflects the mitochondrial respiratory state. Disruption of electron flux at the level of the cytochrome bc<sub>1</sub> complex (cIII) or cytochrome c oxidase (cIV) shifts the Q redox poise to a more reduced state which is generally sensed as respirato  ...[more]

Similar Datasets

Proteomics Complexome profiling of mitochondrial protein complexes in single and double MIC26 and MIC27 knockout cells
2020-07-28 | PXD016733 | Pride
Proteomics Complexome profiling of MICOS complex, impact of subunits MIC26 and MIC27
2020-07-28 | PXD016732 | Pride
Proteomics Complexome profiling of human cybrids laking mitochondrial genes Cox1 or Cox2
2020-07-01 | PXD017840 | Pride
Proteomics Complexome profiling of brain mitochondrial membranes from Clpp-/- mouse
2022-02-17 | PXD025478 | Pride
Proteomics Complexome profiling of mitochondrial protein complexes from patients with mutation in NDUFC2 gene
2020-08-10 | PXD014936 | Pride
Proteomics Complexome profiling of mitochondrial protein complexes from patients with mutation in NDUFAF8 gene
2020-03-05 | PXD015749 | Pride
Proteomics Dynamic complexome profiling identifies impaired protein turnover in mouse CLPP-/-embryonic fibroblasts
2020-03-05 | PXD017463 | Pride
Proteomics Complexome profiling of brain mitochondria from WT and ClpP-/- mice
2024-01-17 | PXD036901 | Pride
Proteomics Complexome profiling of testis tissue in WT and ClpP-/- mice
2024-01-17 | PXD035352 | Pride
Proteomics Complexome profiling of heart mitochondria from WT and ClpP-/- mice
2024-01-17 | PXD036933 | Pride